Structure of PDB 6oi7 Chain C

Receptor sequence
>6oi7C (length=497) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKT
QVFPLERNAAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDEL
TGPFESIVEMSCLMHDIGNPPFGHFGEAAINDWFRQRLHPEDAESQPLTD
DRCSVAALRLRDGEEPLNELRRKIRQDLCHFEGNAQGIRLVHTLMRMNLT
WAQVGGILKYTRPAWWRGETPETHHYLMKKPGYYLSEEAYIARLRKELNL
ALYSRFPLTWIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWGQH
EKGSLFSLVVENAWEKSRSSTEDQFFMYLRVNTLNKLVPYAAQRFIDNLP
AIFAGTFNHALLEDASECSDLLKLYKNVAVKHVFSHPDVERLELQGYRVI
SGLLEIYRPLLSLSLSDFTELVEKERVKRFPIESRLFHKLSTRHRLAYVE
AVSKLPSDSPEFPLWEYYYRCRLLQDYISGMTDLYAWDEYRRLMAVE
3D structure
PDB6oi7 The crystal structure of dGTPase reveals the molecular basis of dGTP selectivity.
ChainC
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H69 H117 D118 D268 R442
Catalytic site (residue number reindexed from 1) H67 H115 D116 D266 R435
Enzyme Commision number 3.1.5.1: dGTPase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MN C H69 H117 D118 D268 H67 H115 D116 D266
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003697 single-stranded DNA binding
GO:0003924 GTPase activity
GO:0008832 dGTPase activity
GO:0016787 hydrolase activity
GO:0016793 triphosphoric monoester hydrolase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0050897 cobalt ion binding
Biological Process
GO:0006203 dGTP catabolic process
GO:0015949 nucleobase-containing small molecule interconversion
GO:0043099 pyrimidine deoxyribonucleoside salvage

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Molecular Function
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Biological Process
External links
PDB RCSB:6oi7, PDBe:6oi7, PDBj:6oi7
PDBsum6oi7
PubMed31019074
UniProtP15723|DGTP_ECOLI Deoxyguanosinetriphosphate triphosphohydrolase (Gene Name=dgt)

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